Evidence map›Paper›PMID 22056329›Full record

ArticleJournal of molecular biology2012

Structure of the glycosyltransferase EryCIII in complex with its activating P450 homologue EryCII.

Martin C Moncrieffe, Maria-Jose Fernandez, Dieter Spiteller, Hiroyoshi Matsumura, Nicholas J Gay, Ben F Luisi, Peter F Leadlay

Abstract read
In one paragraph

Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Non-Canonical Cytochrome P450 Enzymes in Nature.bioRxiv : the preprint server for biology · 2024
    Article
  6. Article
  7. Rethinking Biosynthesis of Aclacinomycin A.Molecules (Basel, Switzerland) · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Unusual cytochrome p450 enzymes and reactions.The Journal of biological chemistry · 2013
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Martin C MoncrieffeDepartment of Biochemistry, Cambridge University, Cambridge CB2 1GA, UK. mcm35@cam.ac.uk
Maria-Jose Fernandez
Dieter Spiteller
Hiroyoshi Matsumura
Nicholas J Gay
Ben F Luisi
Peter F Leadlay

Funding

Biotechnology and Biological Sciences Research Council BB/F023111/1Biotechnology and Biological Sciences Research Council BB/G002797/1Biotechnology and Biological Sciences Research Council BB/G009295/1Medical Research Council G1000133Wellcome Trust 076846/Z/05/AWellcome Trust 100321
6 · The paper itself

Abstract

In the biosynthesis of the clinically important antibiotic erythromycin D, the glycosyltransferase (GT) EryCIII, in concert with its partner EryCII, attaches a nucleotide-activated sugar to the macrolide scaffold with high specificity. To understand the role of EryCII, we have determined the crystal structure of the EryCIII·EryCII complex at 3.1 Å resolution. The structure reveals a heterotetramer with a distinctive, elongated quaternary organization. The EryCIII subunits form an extensive self-complementary dimer interface at the center of the complex, and the EryCII subunits lie on the periphery. EryCII binds in the vicinity of the putative macrolide binding site of EryCIII but does not make direct interactions with this site. Our biophysical and enzymatic data support a model in which EryCII stabilizes EryCIII and also functions as an allosteric activator of the GT.

Indexed as

Allosteric RegulationAmino Acid SequenceAnti-Bacterial AgentsBacterial ProteinsBinding SitesCatalysisCrystallography, X-RayCytochrome P-450 Enzyme SystemErythromycinEscherichia coliGlycosyltransferasesModels, MolecularMolecular Sequence DataOxidoreductasesRecombinant ProteinsSolubilityAnti-Bacterial AgentsBacterial ProteinsCytochrome P-450 Enzyme SystemeryBII protein, Saccharopolyspora erythraeaEryCIII protein, Saccharopolyspora erythraeaErythromycinGlycosyltransferasesOxidoreductasesRecombinant Proteins

Identifiers

PMID22056329
PMCPMC3391682

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.